Fluorescence spectroscopic studies on equilibrium dipole-relaxational dynamics of Na,K-ATPase.

Intramolecular dynamics in Na,K-ATPase molecules have been studied by ultraviolet fluorescence spectroscopic methods: determination of temperature-dependent shifts in steady-state spectra, site-selective red-edge effects and their temperature dependence, and time-resolved emission decay as a function of excitation and emission wavelengths. The combination of these methods allows the characterization of the dipolar-relaxational mobility in the environment of the tryptophan residues. Our results show that the mean dipolar-relaxational time is of the order of one nanosecond at room temperature. This is much faster than what is usually observed in globular proteins. The fast dynamics of the protein dipoles are rapid enough so that the dipoles are in dielectric equilibrium during the slower ion transfer processes; this may have important functional consequences.